DnaK is the hsp70 (a Heat-Shock Protein with a molecular weight of 70 kDa) of Escherichia coli. DnaK plays important roles in the regulation of heat-shock response, partition and cell division. DnaK is also a chaperone protein that has the ability to facilitate the folding of denatured proteins. DnaK has an N-terminal ATPase domain and a C-terminal domain with a peptide binding activity. We have used the 500 MHz proton NMR transferred NOE experiments to study the conformation of the DnaK bound peptide. We have found that the bound peptide is in an extended conformation.